Cilia, KIF3 molecular motor and nodal flow

2012 ◽  
Vol 24 (1) ◽  
pp. 31-39 ◽  
Author(s):  
Nobutaka Hirokawa ◽  
Yosuke Tanaka ◽  
Yasushi Okada
Keyword(s):  
Molecular Motor ◽  
Nodal Flow

scholarly journals Left-Right Determination: Involvement of Molecular Motor KIF3, Cilia, and Nodal Flow

2009 ◽  
Vol 1 (1) ◽  
pp. a000802-a000802 ◽  
Author(s):  
N. Hirokawa ◽  
Y. Tanaka ◽  
Y. Okada
Keyword(s):  
Molecular Motor ◽  
Nodal Flow

scholarly journals A model of processive walking and slipping of kinesin-8 molecular motors

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ping Xie
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
External Load ◽  
Molecular Motor ◽  
Velocity Versus ◽  
Stick Slip ◽  
Load Dependence ◽  
Chemomechanical Coupling ◽  
Similarities And Differences ◽  
Stick Slip Motion

AbstractKinesin-8 molecular motor can move with superprocessivity on microtubules towards the plus end by hydrolyzing ATP molecules, depolymerizing microtubules. The available single molecule data for yeast kinesin-8 (Kip3) motor showed that its superprocessive movement is frequently interrupted by brief stick–slip motion. Here, a model is presented for the chemomechanical coupling of the kinesin-8 motor. On the basis of the model, the dynamics of Kip3 motor is studied analytically. The analytical results reproduce quantitatively the available single molecule data on velocity without including the slip and that with including the slip versus external load at saturating ATP as well as slipping velocity versus external load at saturating ADP and no ATP. Predicted results on load dependence of stepping ratio at saturating ATP and load dependence of velocity at non-saturating ATP are provided. Similarities and differences between dynamics of kinesin-8 and that of kinesin-1 are discussed.

Skeletal Muscle of Molecular Motor and Its Application in Active Rehabilitation of Human Lower Limbs

2021 ◽  
Vol 217 (1) ◽  
pp. 54-68
Author(s):  
Feng Han ◽  
Zhi Yan ◽  
Minjia Wang ◽  
Tong Li ◽  
Jiaqing Li ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Molecular Motor ◽  
Lower Limbs ◽  
Active Rehabilitation

scholarly journals Studies of Conformational Changes of Tubulin Induced by Interaction with Kinesin Using Atomistic Molecular Dynamics Simulations

2021 ◽  
Vol 22 (13) ◽  
pp. 6709
Author(s):  
Xiao-Xuan Shi ◽  
Peng-Ye Wang ◽  
Hong Chen ◽  
Ping Xie
Keyword(s):  
Molecular Dynamics ◽  
High Resolution ◽  
Binding Energy ◽  
Molecular Dynamics Simulations ◽  
Conformational Changes ◽  
Weak Interactions ◽  
Molecular Motor ◽  
Structural Data ◽  
Calculated Binding Energy ◽  
Dynamics Simulations

The transition between strong and weak interactions of the kinesin head with the microtubule, which is regulated by the change of the nucleotide state of the head, is indispensable for the processive motion of the kinesin molecular motor on the microtubule. Here, using all-atom molecular dynamics simulations, the interactions between the kinesin head and tubulin are studied on the basis of the available high-resolution structural data. We found that the strong interaction can induce rapid large conformational changes of the tubulin, whereas the weak interaction cannot. Furthermore, we found that the large conformational changes of the tubulin have a significant effect on the interaction of the tubulin with the head in the weak-microtubule-binding ADP state. The calculated binding energy of the ADP-bound head to the tubulin with the large conformational changes is only about half that of the tubulin without the conformational changes.

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